D
Dorothee Kern
Researcher at Howard Hughes Medical Institute
Publications - 78
Citations - 11539
Dorothee Kern is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Protein structure & Allosteric regulation. The author has an hindex of 38, co-authored 73 publications receiving 10497 citations. Previous affiliations of Dorothee Kern include Brandeis University & University of California, Berkeley.
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Journal ArticleDOI
Dynamic personalities of proteins.
TL;DR: The dream is to 'watch' proteins in action in real time at atomic resolution, which requires addition of a fourth dimension, time, to structural biology so that the positions in space and time of all atoms in a protein can be described in detail.
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Intrinsic dynamics of an enzyme underlies catalysis
Elan Z. Eisenmesser,Oscar Millet,Wladimir Labeikovsky,Dmitry M. Korzhnev,Magnus Wolf-Watz,Magnus Wolf-Watz,Daryl A. Bosco,Daryl A. Bosco,Jack J. Skalicky,Jack J. Skalicky,Lewis E. Kay,Dorothee Kern +11 more
TL;DR: It is shown that the intrinsic plasticity of the protein is a key characteristic of catalysis, and the pre-existence of collective dynamics in enzymes before catalysis is a common feature of biocatalysts and that proteins have evolved under synergy pressure between structure and dynamics.
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A hierarchy of timescales in protein dynamics is linked to enzyme catalysis.
Katherine A. Henzler-Wildman,Ming Lei,Vu Hong Thai,S. Jordan Kerns,Martin Karplus,Dorothee Kern +5 more
TL;DR: It is shown that pico- to nano-second timescale atomic fluctuations in hinge regions of adenylate kinase facilitate the large-scale, slower lid motions that produce a catalytically competent state.
Journal ArticleDOI
Intrinsic motions along an enzymatic reaction trajectory
Katherine A. Henzler-Wildman,Vu Hong Thai,Ming Lei,Maria Ott,Magnus Wolf-Watz,Magnus Wolf-Watz,Timothy D. Fenn,Timothy D. Fenn,Ed Pozharski,Ed Pozharski,Mark A. Wilson,Mark A. Wilson,Gregory A. Petsko,Martin Karplus,Christian G. Hübner,Christian G. Hübner,Dorothee Kern +16 more
TL;DR: In this paper, the authors show evidence for conformational substates along the trajectory towards the catalytically competent 'closed' state in the ligand-free form of the enzyme adenylate kinase.
Journal ArticleDOI
Enzyme dynamics during catalysis.
TL;DR: The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover, which allow a prediction of the reaction trajectory.